Construction and Characterization of a Recombinant Mutant Homolog of the CheW Protein from Thermotoga petrophila RKU-1

Construction and Characterization of a Recombinant Mutant Homolog of the CheW Protein from... In this work, a recombinant chemotaxis CheW protein from Thermotoga petrophila RKU-1 (TpeCheW) and its mutant homologue (TpeCheW-mut) have been obtained. Despite the low homology with the CheW protein of the Escherichia coli bacteria, these proteins do not cause metabolic overload and are well expressed by E. coli laboratory strains. A wide range of features and parameters important for isolation of the TpeCheW-mut protein, such as stability over a wide range of temperatures and pH values, high level of expression, solubility, and the possibility of using simple low-stage purification schemes, including heat pretreatment, has been recognized. Possible directions of using this protein in the practice of scientific and applied research have been formulated and justified. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry Springer Journals

Construction and Characterization of a Recombinant Mutant Homolog of the CheW Protein from Thermotoga petrophila RKU-1

Loading next page...
 
/lp/springer_journal/construction-and-characterization-of-a-recombinant-mutant-homolog-of-Dich5fGiEY
Publisher
Springer Journals
Copyright
Copyright © 2018 by Pleiades Publishing, Ltd.
Subject
Chemistry; Bioorganic Chemistry; Medicinal Chemistry
ISSN
1990-7508
eISSN
1990-7516
D.O.I.
10.1134/S1990750818020051
Publisher site
See Article on Publisher Site

Abstract

In this work, a recombinant chemotaxis CheW protein from Thermotoga petrophila RKU-1 (TpeCheW) and its mutant homologue (TpeCheW-mut) have been obtained. Despite the low homology with the CheW protein of the Escherichia coli bacteria, these proteins do not cause metabolic overload and are well expressed by E. coli laboratory strains. A wide range of features and parameters important for isolation of the TpeCheW-mut protein, such as stability over a wide range of temperatures and pH values, high level of expression, solubility, and the possibility of using simple low-stage purification schemes, including heat pretreatment, has been recognized. Possible directions of using this protein in the practice of scientific and applied research have been formulated and justified.

Journal

Biochemistry (Moscow) Supplement Series B: Biomedical ChemistrySpringer Journals

Published: May 30, 2018

References

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 18 million articles from more than
15,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Search

Query the DeepDyve database, plus search all of PubMed and Google Scholar seamlessly

Organize

Save any article or search result from DeepDyve, PubMed, and Google Scholar... all in one place.

Access

Get unlimited, online access to over 18 million full-text articles from more than 15,000 scientific journals.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve

Freelancer

DeepDyve

Pro

Price

FREE

$49/month
$360/year

Save searches from
Google Scholar,
PubMed

Create lists to
organize your research

Export lists, citations

Read DeepDyve articles

Abstract access only

Unlimited access to over
18 million full-text articles

Print

20 pages / month

PDF Discount

20% off